1yru

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[[Image:1yru.gif|left|200px]]<br /><applet load="1yru" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1yru.gif|left|200px]]
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caption="1yru, resolution 2.50&Aring;" />
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'''Crystal Structure analysis of the adenylyl cyclaes catalytic domain of adenylyl cyclase toxin of Bordetella pertussis in presence of c-terminal calmodulin and 1mM calcium chloride'''<br />
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{{Structure
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|PDB= 1yru |SIZE=350|CAPTION= <scene name='initialview01'>1yru</scene>, resolution 2.50&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Adenylate_cyclase Adenylate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.1 4.6.1.1]
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|GENE= cya, cyaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=520 Bordetella pertussis]), CALM1, CALM2, CALM3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Crystal Structure analysis of the adenylyl cyclaes catalytic domain of adenylyl cyclase toxin of Bordetella pertussis in presence of c-terminal calmodulin and 1mM calcium chloride'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1YRU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bordetella_pertussis Bordetella pertussis] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Adenylate_cyclase Adenylate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.1 4.6.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YRU OCA].
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1YRU is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bordetella_pertussis Bordetella pertussis] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YRU OCA].
==Reference==
==Reference==
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Structural basis for the interaction of Bordetella pertussis adenylyl cyclase toxin with calmodulin., Guo Q, Shen Y, Lee YS, Gibbs CS, Mrksich M, Tang WJ, EMBO J. 2005 Sep 21;24(18):3190-201. Epub 2005 Sep 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16138079 16138079]
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Structural basis for the interaction of Bordetella pertussis adenylyl cyclase toxin with calmodulin., Guo Q, Shen Y, Lee YS, Gibbs CS, Mrksich M, Tang WJ, EMBO J. 2005 Sep 21;24(18):3190-201. Epub 2005 Sep 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16138079 16138079]
[[Category: Adenylate cyclase]]
[[Category: Adenylate cyclase]]
[[Category: Bordetella pertussis]]
[[Category: Bordetella pertussis]]
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[[Category: cyaa]]
[[Category: cyaa]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:08:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:26:41 2008''

Revision as of 13:26, 20 March 2008

Image:1yru.gif


PDB ID 1yru

Drag the structure with the mouse to rotate
, resolution 2.50Å
Ligands:
Gene: cya, cyaA (Bordetella pertussis), CALM1, CALM2, CALM3 (Homo sapiens)
Activity: Adenylate cyclase, with EC number 4.6.1.1
Coordinates: save as pdb, mmCIF, xml



Crystal Structure analysis of the adenylyl cyclaes catalytic domain of adenylyl cyclase toxin of Bordetella pertussis in presence of c-terminal calmodulin and 1mM calcium chloride


Contents

Overview

CyaA is crucial for colonization by Bordetella pertussis, the etiologic agent of whooping cough. Here we report crystal structures of the adenylyl cyclase domain (ACD) of CyaA with the C-terminal domain of calmodulin. Four discrete regions of CyaA bind calcium-loaded calmodulin with a large buried contact surface. Of those, a tryptophan residue (W242) at an alpha-helix of CyaA makes extensive contacts with the calcium-induced, hydrophobic pocket of calmodulin. Mutagenic analyses show that all four regions of CyaA contribute to calmodulin binding and the calmodulin-induced conformational change of CyaA is crucial for catalytic activation. A crystal structure of CyaA-calmodulin with adefovir diphosphate, the metabolite of an approved antiviral drug, reveals the location of catalytic site of CyaA and how adefovir diphosphate tightly binds CyaA. The ACD of CyaA shares a similar structure and mechanism of activation with anthrax edema factor (EF). However, the interactions of CyaA with calmodulin completely diverge from those of EF. This provides molecular details of how two structurally homologous bacterial toxins evolved divergently to bind calmodulin, an evolutionarily conserved calcium sensor.

Disease

Known diseases associated with this structure: Cavernous malformations of CNS and retina OMIM:[604214], Cerebral cavernous malformations-1 OMIM:[604214], Hyperkeratotic cutaneous capillary-venous malformations associated with cerebral capillary malformations OMIM:[604214], Leukemia, acute T-cell lymphoblastic OMIM:[603025], Leukemia, acute myeloid OMIM:[603025]

About this Structure

1YRU is a Protein complex structure of sequences from Bordetella pertussis and Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for the interaction of Bordetella pertussis adenylyl cyclase toxin with calmodulin., Guo Q, Shen Y, Lee YS, Gibbs CS, Mrksich M, Tang WJ, EMBO J. 2005 Sep 21;24(18):3190-201. Epub 2005 Sep 1. PMID:16138079

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